Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Regulation of the rhodopsin-transducin interaction by a highly conserved carboxylic acid group.

Biochemistry - 20 Jul 1993

Fahmy K, Sakmar T P

Abstract excerpt

Rhodopsin is a member of a family of G protein-coupled receptors which share structural and functional homologies. A tripeptide sequence (Glu or Asp/Arg/Tyr) at the cytoplasmic border of the third transmembrane segment is conserved among most of these receptors. This region is involved in G protein activation in rhodopsin as well as in other receptors. The role of the conserved Glu-134 was studied by...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Amino Acid Sequence
Share to Conserved Sequence
Share to Hydrogen-Ion Concentration

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Kinetics

Share to Molecular Sequence Data

Share to Mutation

Share to Recombinant Proteins

Source

Identifiers

PMID: 8343512
DOI: 10.1021/bi00079a020

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026. Manifest publication-graph-cohort-2026-09-05.1.

Source receipt: pubmed, retrieved 5 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Regulation of the rhodopsin-transducin interaction by a highly conserved carboxylic acid group.PMID 8343512Read ↗

Constitutive activation of opsin: influence of charge at position 134 and size at position 296.Semantic proximity Read ↗

Contribution of glutamic acid in the conserved E/DRY triad to the functional properties of rhodopsin.Semantic proximity Read ↗

Critical role of electrostatic interactions of amino acids at the cytoplasmic region of helices 3 and 6 in rhodopsin conformational properties and activation.Semantic proximity Read ↗

Movement of the retinylidene Schiff base counterion in rhodopsin by one helix turn reverses the pH dependence of the metarhodopsin I to metarhodopsin II transition.Semantic proximity Read ↗

Rhodopsin activation exposes a key hydrophobic binding site for the transducin alpha-subunit C terminus.Semantic proximity Read ↗

Rhodopsin determinants for transducin activation: a gain-of-function approach.Semantic proximity Read ↗

Structural impact of the E113Q counterion mutation on the activation and deactivation pathways of the G protein-coupled receptor rhodopsin.Semantic proximity Read ↗

Structure and function in rhodopsin: rhodopsin mutants with a neutral amino acid at E134 have a partially activated conformation in the dark state.Semantic proximity Read ↗

Receptor and betagamma binding sites in the alpha subunit of the retinal G protein transducin.Semantic proximity Read ↗

Light-dependent transducin activation by an ultraviolet-absorbing rhodopsin mutant.Semantic proximity Read ↗

Opsins with mutations at the site of chromophore attachment constitutively activate transducin but are not phosphorylated by rhodopsin kinase.Semantic proximity Read ↗

Mutational analysis of the pleckstrin homology domain of the beta-adrenergic receptor kinase. Differential effects on G beta gamma and phosphatidylinositol 4,5-bisphosphate binding.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.